3T0C

Crystal structure of Streptococcus mutans MetE complexed with Zinc

「3L7S」から置き換えられました

3T0C の概要

• エントリーDOI: 10.2210/pdb3t0c/pdb
• 関連するPDBエントリー: 2NQ5 3L7R
• 分子名称: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase, SULFATE ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: mete, barrel, methyltransferase, transferase
• 由来する生物種: Streptococcus mutans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 88153.42

構造登録者

Fu, T.M.,Liang, Y.H.,Su, X.D. (登録日: 2011-07-19, 公開日: 2011-08-03, 最終更新日: 2023-11-01)

主引用文献

Fu, T.M.,Almqvist, J.,Liang, Y.H.,Li, L.,Huang, Y.,Su, X.D.
Crystal Structures of Cobalamin-Independent Methionine Synthase (MetE) from Streptococcus mutans: A Dynamic Zinc-Inversion Model
J.Mol.Biol., 412:688-697, 2011

PubMed Abstract: Cobalamin-independent methionine synthase (MetE) catalyzes the direct transfer of a methyl group from methyltetrahydrofolate to l-homocysteine to form methionine. Previous studies have shown that the MetE active site coordinates a zinc atom, which is thought to act as a Lewis acid and plays a role in the activation of thiol. Extended X-ray absorption fine structure studies and mutagenesis experiments identified the zinc-binding site in MetE from Escherichia coli. Further structural investigations of MetE from Thermotoga maritima lead to the proposition of two models: "induced fit" and "dynamic equilibrium", to account for the catalytic mechanisms of MetE. Here, we present crystal structures of oxidized and zinc-replete MetE from Streptococcus mutans at the physiological pH. The structures reveal that zinc is mobile in the active center and has the possibility to invert even in the absence of homocysteine. These structures provide evidence for the dynamic equilibrium model.

PubMed: 21840320
DOI: 10.1016/j.jmb.2011.08.005

実験手法

X-RAY DIFFRACTION (2.187 Å)